Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP6 inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2α) with a dissociation constant of (Kd) of 4 nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2α-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2α and deletion mutants of Nopp140. InsP6 specifically binds to CK2α and disrupts the interaction between CK2α and Nopp140 with an IC50 value of 25 μM, thereby attenuating the Nopp140-mediated repression of CK2 activity.
|Number of pages||6|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 2008 Nov 14|
Bibliographical noteFunding Information:
This work was supported by a grant from the Functional Proteomics Research (FPR05B2040), Ministry of Science and Technology, and by the Korea Research Foundation Grant (KRF-2006-C00137), funded by the Korean Government (MOEHRD).
- Protein interaction
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology